Application and properties of butyl acrylate/pentaerythrite triacrylate copolymers and cellulose-based Granocel as carriers for trypsin immobilization

Bryjak, Jolanta; Liesienė, Jolanta; Kolarz, Bożena N.

doi:10.1016/j.colsurfb.2007.07.006

Cited by 29 publications

(15 citation statements)

References 31 publications

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“…Similar results and preferences for Granocel-carriers superstructure and modification were observed after immobilization of glucoamylase and laccase (Rekuć et al 2007). From the other hand, immobilization of trypsin on Granocel carriers revealed preference to DVS activation of non-modified carrier (Bryjak et al 2008).…”

Section: Discussionsupporting

confidence: 85%

Man-tailored cellulose-based carriers for invertase immobilization

2008

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Cellulose-based carriers Granocel were specially prepared and optimised for covalent immobilization of enzymes. The effects of carrier characteristics such as pore size, chemistry of anchor groups and their density on invertase immobilization efficiency were evaluated. It was found that the preferential adsorption/binding of the enzyme to a carrier during coupling and its activity after immobilization depended on microenvironmental effects created by hydrophilic surface of the carrier, functional groups and their activators. The best preparations (activity approx. 300 U/mL, high storage stability) were obtained for NH 2 -Granocel activated with glutaraldehyde. It is probably due to Granocel modification with pentaethylenehexamine that gave a 19-atom spacer arm. The enzyme concentration in coupling mixture was optimised as well. The kinetic parameters of sucrose hydrolysis for native and immobilized invertase were evaluated. Compared to the native invertase, K m value of immobilized enzyme was only twice higher with about three times lower substrate inhibition. Reaction runs in a well mixed batch reactors with native and immobilized invertase showed slightly slower reaction rate in the case of the enzyme covalently bound to Granocel. Very good stability of cellulose-based carrier was proved experimentally by 20 successive reaction runs in a batch reactor.

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Section: Discussionsupporting

confidence: 85%

Man-tailored cellulose-based carriers for invertase immobilization

2008

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“…Bryjak et al also compared different activation Fig. 6 Operational stability comparisons of immobilized and native trypsin systems methods for trypsin covalent immobilization on acrylic series carriers, and immobilization efficiencies of the protein and the activity could reach 65.0% and 26.5%, respectively [20]. In this particular study, however, trypsin was immobilized on pH-dependent p(AAc/ MBA) hydrogel microspheres through modified adsorption method.…”

Section: Presents Thementioning

confidence: 94%

“…The p(AAc/MBA) microspheres, among the most widely used and simplest polyacid hydrogels, were applied as the supports for alkaline enzymes. Trypsin was selected as the model owing to its appropriate activity pH range and to the considerable academic interest it has gained [18][19][20]. When the system used for catalysis at pH 8.0, conjugated trypsin can be released, while at pH 4.0, the catalysis reaction was almost impeded and trypsin was reloaded after a while.…”

Section: Introductionmentioning

confidence: 99%

A Novel Reversible pH-Triggered Release Immobilized Enzyme System

Gai

2008

Appl Biochem Biotechnol

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A novel immobilized enzyme system supported by poly(acrylic acid/N,N'-methylene-bisacryl-amide) hydrogel microspheres was prepared. This system exhibited characteristics of reversible pH-triggered release. The morphology, size, and chemical structure were examined through optical microscopy, particle size analyzer, and Fourier transform infrared spectrometer. Immobilization and release features were further investigated under different conditions, including pH, time, and microsphere quantity. Results showed the microspheres were regularly spherical with 3.8 approximately 6.6 microm diameter. Loading efficiencies of bovine serum albumin immobilized by gel entrapment and adsorption methods were 93.9% and 56.2%, respectively. The pH-triggered protein release of the system occurred when medium pH was above 6.0, while it was hardly detected when medium pH was below 6.0. Release efficiencies of entrapped and adsorbed protein were 6.38% and 95.0%, respectively. Hence, adsorption method was used to immobilize trypsin. Loading efficiency of 77.2% was achieved at pH 4.0 in 1 h. Release efficiency of 91.6% was obtained under optimum pH catalysis condition set at 8.0 and trypsin was free in solutions with retention activity of 63.3%. And 51.5% of released trypsin could be reloaded in 10 min. The results indicate this kind of immobilized enzyme system offers a promising alternative for enzyme recovery in biotechnology.

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“…Among the many methods of immobilization (e.g. adsorption, entrapment, electrostatic interaction and covalent binding) the covalent binding of enzymes to water-insoluble carriers seems to be the most attractive method for enzyme stabilization, reusability and recovery [11]. The immobilization of enzymes has been a booming field of research due to its advantages for the recovery and reuse of higher cost enzymes and for the easier separation of enzymes from catalytic product, as well as in the improvement of the enzymes' stability in both storage and operational processes [12].…”

Section: Introductionmentioning

confidence: 99%